Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction.
Identifieur interne : 002416 ( PubMed/Corpus ); précédent : 002415; suivant : 002417Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction.
Auteurs : Tin-Yun Ho ; Shih-Lu Wu ; Jaw-Chyun Chen ; Yen-Chiao Wei ; Shin-Ei Cheng ; Yung-Hsien Chang ; Hsu-Jan Liu ; Chien-Yun HsiangSource :
- Antiviral research [ 0166-3542 ] ; 2006.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Biotinylation, Chlorocebus aethiops, DNA-Binding Proteins (antagonists & inhibitors), DNA-Binding Proteins (metabolism), Enzyme-Linked Immunosorbent Assay, Humans, Membrane Glycoproteins (antagonists & inhibitors), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Molecular Sequence Data, Peptides (chemical synthesis), Peptides (chemistry), Peptides (metabolism), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), SARS Virus (metabolism), SARS Virus (pathogenicity), Saccharomyces cerevisiae Proteins (antagonists & inhibitors), Saccharomyces cerevisiae Proteins (metabolism), Severe Acute Respiratory Syndrome (virology), Spike Glycoprotein, Coronavirus, Transcription Factors (antagonists & inhibitors), Transcription Factors (metabolism), Vero Cells, Viral Envelope Proteins (antagonists & inhibitors), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , antagonists & inhibitors : DNA-Binding Proteins, Membrane Glycoproteins, Saccharomyces cerevisiae Proteins, Transcription Factors, Viral Envelope Proteins.
- chemical , chemical synthesis : Peptides.
- chemical , chemistry : Membrane Glycoproteins, Peptides, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , metabolism : DNA-Binding Proteins, Membrane Glycoproteins, Peptides, Recombinant Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors, Viral Envelope Proteins.
- metabolism : SARS Virus.
- pathogenicity : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Amino Acid Sequence, Animals, Biotinylation, Chlorocebus aethiops, Enzyme-Linked Immunosorbent Assay, Humans, Molecular Sequence Data, Spike Glycoprotein, Coronavirus, Vero Cells.
Abstract
Severe acute respiratory syndrome (SARS) is an emerging infectious disease caused by a novel coronavirus (SARS-CoV). The binding of SARS-CoV spike (S) protein to cellular angiotensin-converting enzyme 2 (ACE2) is the first step in SARS-CoV infection. Therefore, we assayed the inhibitory effects of small peptides derived from S protein on the binding of S protein to ACE2 and on the S-protein-pseudotyped retrovirus infectivity. SP-4 (residues 192-203), SP-8 (residues 483-494), and SP-10 (residues 668-679) significantly blocked the interaction between S protein and ACE2 by biotinylated enzyme-linked immunosorbent assay, with IC(50) values of 4.30 +/- 2.18, 6.99 +/- 0.71, and 1.88 +/- 0.52 nmol, respectively. Peptide scanning suggested the region spanning residues 660-683 might act as a receptor-binding domain. SP-10 blocked both binding of the S protein and infectivity of S protein-pseudotyped retrovirus to Vero E6 cells. In conclusion, this is the first report of small peptides designed to disrupt the binding of SARS-CoV S protein to ACE2. Our findings suggest that SP-10 may be developed as an anti-SARS-CoV agent for the treatment of SARS-CoV infection.
DOI: 10.1016/j.antiviral.2005.10.005
PubMed: 16337697
Links to Exploration step
pubmed:16337697Le document en format XML
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for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction.</title><author><name sortKey="Ho, Tin Yun" sort="Ho, Tin Yun" uniqKey="Ho T" first="Tin-Yun" last="Ho">Tin-Yun Ho</name><affiliation><nlm:affiliation>Molecular Biology Laboratory, Graduate Institute of Chinese Medical Science, China Medical University, Taichung, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Wu, Shih Lu" sort="Wu, Shih Lu" uniqKey="Wu S" first="Shih-Lu" last="Wu">Shih-Lu Wu</name></author><author><name sortKey="Chen, Jaw Chyun" sort="Chen, Jaw Chyun" uniqKey="Chen J" first="Jaw-Chyun" last="Chen">Jaw-Chyun Chen</name></author><author><name sortKey="Wei, Yen Chiao" sort="Wei, Yen Chiao" uniqKey="Wei Y" first="Yen-Chiao" last="Wei">Yen-Chiao Wei</name></author><author><name sortKey="Cheng, Shin Ei" sort="Cheng, Shin Ei" uniqKey="Cheng S" first="Shin-Ei" last="Cheng">Shin-Ei Cheng</name></author><author><name sortKey="Chang, Yung Hsien" sort="Chang, Yung Hsien" uniqKey="Chang Y" first="Yung-Hsien" last="Chang">Yung-Hsien Chang</name></author><author><name sortKey="Liu, Hsu Jan" sort="Liu, Hsu Jan" uniqKey="Liu H" first="Hsu-Jan" last="Liu">Hsu-Jan Liu</name></author><author><name sortKey="Hsiang, Chien Yun" sort="Hsiang, Chien Yun" uniqKey="Hsiang C" first="Chien-Yun" last="Hsiang">Chien-Yun Hsiang</name></author></analytic><series><title level="j">Antiviral research</title><idno type="ISSN">0166-3542</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Biotinylation</term><term>Chlorocebus aethiops</term><term>DNA-Binding Proteins (antagonists & inhibitors)</term><term>DNA-Binding Proteins (metabolism)</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Humans</term><term>Membrane Glycoproteins (antagonists & inhibitors)</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (metabolism)</term><term>Molecular Sequence Data</term><term>Peptides (chemical synthesis)</term><term>Peptides (chemistry)</term><term>Peptides (metabolism)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>SARS Virus (metabolism)</term><term>SARS Virus (pathogenicity)</term><term>Saccharomyces cerevisiae Proteins (antagonists & inhibitors)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Transcription Factors (antagonists & inhibitors)</term><term>Transcription Factors (metabolism)</term><term>Vero Cells</term><term>Viral Envelope Proteins (antagonists & inhibitors)</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>DNA-Binding Proteins</term><term>Membrane Glycoproteins</term><term>Saccharomyces cerevisiae Proteins</term><term>Transcription Factors</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Peptides</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA-Binding Proteins</term><term>Membrane Glycoproteins</term><term>Peptides</term><term>Recombinant Proteins</term><term>Saccharomyces cerevisiae Proteins</term><term>Transcription Factors</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Biotinylation</term><term>Chlorocebus aethiops</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Humans</term><term>Molecular Sequence Data</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) is an emerging infectious disease caused by a novel coronavirus (SARS-CoV). The binding of SARS-CoV spike (S) protein to cellular angiotensin-converting enzyme 2 (ACE2) is the first step in SARS-CoV infection. Therefore, we assayed the inhibitory effects of small peptides derived from S protein on the binding of S protein to ACE2 and on the S-protein-pseudotyped retrovirus infectivity. SP-4 (residues 192-203), SP-8 (residues 483-494), and SP-10 (residues 668-679) significantly blocked the interaction between S protein and ACE2 by biotinylated enzyme-linked immunosorbent assay, with IC(50) values of 4.30 +/- 2.18, 6.99 +/- 0.71, and 1.88 +/- 0.52 nmol, respectively. Peptide scanning suggested the region spanning residues 660-683 might act as a receptor-binding domain. SP-10 blocked both binding of the S protein and infectivity of S protein-pseudotyped retrovirus to Vero E6 cells. In conclusion, this is the first report of small peptides designed to disrupt the binding of SARS-CoV S protein to ACE2. Our findings suggest that SP-10 may be developed as an anti-SARS-CoV agent for the treatment of SARS-CoV infection.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16337697</PMID><DateCompleted><Year>2006</Year><Month>06</Month><Day>06</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0166-3542</ISSN><JournalIssue CitedMedium="Print"><Volume>69</Volume><Issue>2</Issue><PubDate><Year>2006</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Antiviral research</Title><ISOAbbreviation>Antiviral Res.</ISOAbbreviation></Journal><ArticleTitle>Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction.</ArticleTitle><Pagination><MedlinePgn>70-6</MedlinePgn></Pagination><Abstract><AbstractText>Severe acute respiratory syndrome (SARS) is an emerging infectious disease caused by a novel coronavirus (SARS-CoV). The binding of SARS-CoV spike (S) protein to cellular angiotensin-converting enzyme 2 (ACE2) is the first step in SARS-CoV infection. Therefore, we assayed the inhibitory effects of small peptides derived from S protein on the binding of S protein to ACE2 and on the S-protein-pseudotyped retrovirus infectivity. SP-4 (residues 192-203), SP-8 (residues 483-494), and SP-10 (residues 668-679) significantly blocked the interaction between S protein and ACE2 by biotinylated enzyme-linked immunosorbent assay, with IC(50) values of 4.30 +/- 2.18, 6.99 +/- 0.71, and 1.88 +/- 0.52 nmol, respectively. Peptide scanning suggested the region spanning residues 660-683 might act as a receptor-binding domain. SP-10 blocked both binding of the S protein and infectivity of S protein-pseudotyped retrovirus to Vero E6 cells. In conclusion, this is the first report of small peptides designed to disrupt the binding of SARS-CoV S protein to ACE2. Our findings suggest that SP-10 may be developed as an anti-SARS-CoV agent for the treatment of SARS-CoV infection.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ho</LastName><ForeName>Tin-Yun</ForeName><Initials>TY</Initials><AffiliationInfo><Affiliation>Molecular Biology Laboratory, Graduate Institute of Chinese Medical Science, China Medical University, Taichung, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Shih-Lu</ForeName><Initials>SL</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Jaw-Chyun</ForeName><Initials>JC</Initials></Author><Author ValidYN="Y"><LastName>Wei</LastName><ForeName>Yen-Chiao</ForeName><Initials>YC</Initials></Author><Author ValidYN="Y"><LastName>Cheng</LastName><ForeName>Shin-Ei</ForeName><Initials>SE</Initials></Author><Author ValidYN="Y"><LastName>Chang</LastName><ForeName>Yung-Hsien</ForeName><Initials>YH</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Hsu-Jan</ForeName><Initials>HJ</Initials></Author><Author ValidYN="Y"><LastName>Hsiang</LastName><ForeName>Chien-Yun</ForeName><Initials>CY</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>11</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Antiviral Res</MedlineTA><NlmUniqueID>8109699</NlmUniqueID><ISSNLinking>0166-3542</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C066778">ACE2 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004268">DNA-Binding 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UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578557">spike glycoprotein, SARS-CoV</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019921" MajorTopicYN="N">Biotinylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004797" 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MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014709" MajorTopicYN="N">Vero Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" 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